Isolation and characterization of an arylalkylamine N‐acetyltransferase from Drosophila melanogaster

FEBS Letters

Meyer, Urs A.²  Hintermann, Edith²  Jenö, Paul¹ 

[1] Department of Biochemistry, Biozentrum of University of Basel, CH-4056 Basel, Switzerland;Department of Pharmacology, Biozentrum of University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland

关键词: Arylalkylamine N-acetyltransferase (aaNAT);    Melatonin;    Pineal gland;    Evolution;    Invertebrate;    Drosophila melanogaster;   

DOI  :  10.1016/0014-5793(95)01198-N

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The enzyme arylalkylamine N-acetyltransferase (aaNAT) catalyzes the rate-limiting step in melatonin formation in the vertebrate pineal gland. Numerous attempts to purify this highly unstable enzyme from vertebrates have been unsuccessful. Here, we report the purification of an aaNAT enzyme from Drosophila melanogaster, using a radioenzymatic activity assay and column chromatography. The isolated 29.5-kDa protein acetylates tryptamine, dopamine and serotonin with affinities of 0.89 to 0.97 mM, respectively. This suggests that the identified aaNAT may be involved in melatonin synthesis and sclerotization as well as in neurotransmitter catabolism in insects.

【 授权许可】

Unknown